Structure of PDB 4ypa Chain C

Receptor sequence

>4ypaC (length=217) Species: 9606 (Homo sapiens)

GAMAGSYKKIRSNVYVDVKPLSGYEATTCNCKKPDDDTRKGCVDDCLNRM
IFAECSPNTCPCGEQCCNQRIQRHEWVQCLERFRAEEKGWGIRTKEPLKA
GQFIIEYLGEVVSEQEFRNRMIEQYHNHSDHYCLNLDSGMVIDSYRMGNE
ARFINHSCDPNCEMQKWSVNGVYRIGLYALKDMPAGTELTYDYNFHSFNV
EKAQLCKCGFEKCRGII

3D structure

• PDB: 4ypa Two Loops Undergoing Concerted Dynamics Regulate the Activity of the ASH1L Histone Methyltransferase.
• Chain: C
• Resolution: 2.3 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): Y2169 Y2255
• Catalytic site (residue number reindexed from 1): Y107 Y193
• Enzyme Commision number: 2.1.1.359: [histone H3]-lysine(36) N-trimethyltransferase.
  2.1.1.367: [histone H3]-lysine(9) N-methyltransferase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	ZN	C	C2091 C2093 C2104 C2108	C29 C31 C42 C46
BS02	ZN	C	C2104 C2117 C2122 C2128	C42 C55 C60 C66
BS03	ZN	C	C2220 C2268 C2270 C2275	C158 C206 C208 C213
BS04	SAM	C	K2150 G2151 W2152 D2192 H2193 Y2194 R2214 F2215 N2217 H2218 Y2255 Q2266 C2268 K2269 I2279	K88 G89 W90 D130 H131 Y132 R152 F153 N155 H156 Y193 Q204 C206 K207 I217

Gene Ontology

Molecular Function

• GO:0042054 histone methyltransferase activity

Cellular Component

• GO:0005634 nucleus

External links

• PDB: RCSB:4ypa, PDBe:4ypa, PDBj:4ypa
• PDBsum: 4ypa
• PubMed: 26292256
• UniProt: Q9NR48|ASH1L_HUMAN Histone-lysine N-methyltransferase ASH1L (Gene Name=ASH1L)